6cmy

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'''Unreleased structure'''
 
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The entry 6cmy is ON HOLD until Paper Publication
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==Solution NMR Structure Determination of Mouse Melanoregulin==
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<StructureSection load='6cmy' size='340' side='right' caption='[[6cmy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6cmy]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5kbo 5kbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CMY FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmy OCA], [http://pdbe.org/6cmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cmy RCSB], [http://www.ebi.ac.uk/pdbsum/6cmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MREG_MOUSE MREG_MOUSE]] Plays a role in the incorporation of pigments into hair. May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells.<ref>PMID:15550542</ref> <ref>PMID:17260955</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Melanoregulin (Mreg) is a small, highly charged, multiply palmitoylated protein present on the membrane of melanosomes. Mreg is implicated in the transfer of melanosomes from melanocytes to keratinocytes, and in promoting the microtubule minus end-directed transport of these organelles. The possible molecular function of Mreg was identified by solving its structure using nuclear magnetic resonance (NMR) spectroscopy. Mreg contains six alpha helices forming a fishhook-like fold in which positive and negative charges occupy opposite sides of the protein's surface and sandwich a putative, cholesterol recognition sequence (CRAC motif). Mreg containing a point mutation within its CRAC motif still targets to late endosomes/lysosomes, but no longer promotes their microtubule minus end-directed transport. Moreover, wild-type Mreg does not promote the microtubule minus end-directed transport of late endosomes/lysosomes in cells transiently depleted of cholesterol. Finally, reversing the charge of three clustered acidic residues partially inhibits Mreg's ability to drive these organelles to microtubule minus ends.
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Authors: Rout, A.K., Wu, X., Strub, M.P., Starich, M.R., Hammer III, J.A., Tjandra, N.
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The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function.,Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147<ref>PMID:30174147</ref>
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Description: Solution NMR Structure Determination of Mouse Melanoregulin
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wu, X]]
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<div class="pdbe-citations 6cmy" style="background-color:#fffaf0;"></div>
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[[Category: Starich, M.R]]
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== References ==
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[[Category: Hammer Iii, J.A]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: III, J A.Hammer]]
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[[Category: Rout, A K]]
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[[Category: Starich, M R]]
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[[Category: Strub, M P]]
[[Category: Tjandra, N]]
[[Category: Tjandra, N]]
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[[Category: Rout, A.K]]
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[[Category: Wu, X]]
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[[Category: Strub, M.P]]
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[[Category: Alpha helical]]
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[[Category: Cellular pigementation]]
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[[Category: Crac motif]]
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[[Category: Dilute suppressor locus]]
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[[Category: Lipid binding protein]]
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[[Category: Melanosome transport]]

Revision as of 19:33, 19 September 2018

Solution NMR Structure Determination of Mouse Melanoregulin

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